MCCA_RAT
ID MCCA_RAT Reviewed; 715 AA.
AC Q5I0C3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000250|UniProtKB:Q96RQ3};
DE Short=MCCase subunit alpha {ECO:0000250|UniProtKB:Q96RQ3};
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1 {ECO:0000250|UniProtKB:Q96RQ3};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000250|UniProtKB:Q96RQ3};
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000250|UniProtKB:Q96RQ3};
DE Flags: Precursor;
GN Name=Mccc1 {ECO:0000312|EMBL:AAH88473.1, ECO:0000312|RGD:1310615};
GN Synonyms=Mcca {ECO:0000250|UniProtKB:Q96RQ3};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH88473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH88473.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
CC carboxylase, an enzyme that catalyzes the conversion of 3-
CC methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC leucine and isovaleric acid catabolism. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q96RQ3};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000250|UniProtKB:Q96RQ3};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits (MCCC1) and six beta (MCCC2) subunits. Interacts (via the
CC biotin carboxylation domain) with SIRT4 (By similarity).
CC {ECO:0000250|UniProtKB:Q96RQ3, ECO:0000250|UniProtKB:Q99MR8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q96RQ3}.
CC -!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q99MR8}.
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DR EMBL; BC088473; AAH88473.1; -; mRNA.
DR RefSeq; NP_001009653.1; NM_001009653.1.
DR AlphaFoldDB; Q5I0C3; -.
DR SMR; Q5I0C3; -.
DR BioGRID; 254844; 1.
DR STRING; 10116.ENSRNOP00000018942; -.
DR iPTMnet; Q5I0C3; -.
DR PhosphoSitePlus; Q5I0C3; -.
DR jPOST; Q5I0C3; -.
DR PaxDb; Q5I0C3; -.
DR PRIDE; Q5I0C3; -.
DR GeneID; 294972; -.
DR KEGG; rno:294972; -.
DR UCSC; RGD:1310615; rat.
DR CTD; 56922; -.
DR RGD; 1310615; Mccc1.
DR eggNOG; KOG0238; Eukaryota.
DR InParanoid; Q5I0C3; -.
DR OrthoDB; 254436at2759; -.
DR PhylomeDB; Q5I0C3; -.
DR BRENDA; 6.4.1.4; 5301.
DR Reactome; R-RNO-196780; Biotin transport and metabolism.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:Q5I0C3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; ISO:RGD.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Biotin; Ligase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 39..715
FT /note="Methylcrotonoyl-CoA carboxylase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000365095"
FT DOMAIN 45..490
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255"
FT DOMAIN 163..360
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 622..711
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 335
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR8"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR8"
FT MOD_RES 490
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR8"
FT MOD_RES 577
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MR8"
FT MOD_RES 577
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99MR8"
FT MOD_RES 677
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 715 AA; 79330 MW; 20FB2EAB8664AD8F CRC64;
MAAAALLAAV DRNQLRRVPI LLLQPREWPW KHRTVKYGTT PGGSITKVLI ANRGEIACRV
IRTARKMGVQ SVAVYSEADR NSMHVDMADE AYSIGPAPSQ QSYLAMEKII QVAKSSAAQA
IHPGYGFLSE NMEFAEFCKQ EGIIFIGPPS TAIRDMGIKS TSKSIMAAAG VPVVEGYHGN
DQSDECLKEH AGKIGYPVMI KAIRGGGGKG MRIIRSEKEF QEQLESARRE AKKSFNDDAM
LIEKFVDTPR HVEVQVFGDH HGNAVYLFER DCSVQRRHQK IIEEAPAPGI DPEVRRRLGE
AAVRAAKAVN YVGAGTVEFI MDSKHNFYFM EMNTRLQVEH PVTEMITGTD LVEWQLRIAA
GEKIPLSQEE IPLQGHAFEA RIYAEDPDNN FMPGAGPLVH LSTPPPDMST RIETGVRQGD
EVSVHYDPMI AKLVVWASDR QSALSKLRYS LHQYNIVGLR TNVDFLLRLS GHSEFEAGNV
HTDFIPQHHK DLLPTHSTIA KESVCQAALG LILKEKEMTS AFKLHTQDQF SPFSFSSGRR
LNISYTRNMT LRSGKNDIII AVTYNRDGSY DMQIENKLFR VLGDLSNEDG YTYLKSSVNG
VASKSKFILL DNTIYLFSME GSIEVGIPVP KYLSPVSAEG TQGGTIAPMT GTIEKVFVKA
GDRVKAGDAL MVMIAMKMEH TIKAPKDGRI KKVFFSEGAQ ANRHAPLVEF EEEEV
